Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q92506: Variant p.Val158Leu

(3R)-3-hydroxyacyl-CoA dehydrogenase
Gene: HSD17B8
Feedback?
Variant information Variant position: help 158 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help US The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change: help From Valine (V) to Leucine (L) at position 158 (V158L, p.Val158Leu). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description: help In a breast cancer sample; somatic mutation. Any additional useful information about the variant.


Sequence information Variant position: help 158 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 261 The length of the canonical sequence.
Location on the sequence: help AAQALVSNGCRGSIINISSI V GKVGNVGQTNYAASKAGVIG The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         AAQALVSNGCRGSIINISSIVGKVGNVGQTNYAASKAGVIG

                              AAQALVSSGCRGSIINISSIVGKVGNVGQTNYAASKAGVIG

Mouse                         AAQALVSSGGRGSIINISSIIGKVGNIGQTNYASSKAGVIG

Rat                           AAQALVSSGGRGSIINISSIVGKVGNIGQTNYASSKAGVIG

Pig                           AAQALVSSGCPGSIINISSIIGKVGNMGQTNYAASKAGVIG

Sequence annotation in neighborhood: help The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.
TypePositionsDescription
Chain 1 – 261 (3R)-3-hydroxyacyl-CoA dehydrogenase
Active site 169 – 169 Proton acceptor
Binding site 156 – 156
Modified residue 160 – 160 N6-succinyllysine
Modified residue 173 – 173 N6-succinyllysine
Mutagenesis 148 – 148 R -> E. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
Mutagenesis 169 – 169 Y -> A. Strongly reduced NADH-dependent reductase activity with acetoacetyl-CoA. Strongly reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Decreases NADPH-dependent reductase activity with acetoacetyl-CoA, but increases NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
Mutagenesis 173 – 173 K -> A. Abolishes NADH-dependent reductase activity with acetoacetyl-CoA. Strongly reduced NADH-dependent reductase activity with 9,10-phenanthrene quinone. Slightly decreases NADPH-dependent reductase activity with acetoacetyl-CoA, but increases NADPH-dependent reductase activity with 9,10-phenanthrene quinone. No effect on the ability to restore growth of an OAR1-deficient yeast mutant.
Helix 158 – 161



Literature citations
The consensus coding sequences of human breast and colorectal cancers.
Sjoeblom T.; Jones S.; Wood L.D.; Parsons D.W.; Lin J.; Barber T.D.; Mandelker D.; Leary R.J.; Ptak J.; Silliman N.; Szabo S.; Buckhaults P.; Farrell C.; Meeh P.; Markowitz S.D.; Willis J.; Dawson D.; Willson J.K.V.; Gazdar A.F.; Hartigan J.; Wu L.; Liu C.; Parmigiani G.; Park B.H.; Bachman K.E.; Papadopoulos N.; Vogelstein B.; Kinzler K.W.; Velculescu V.E.;
Science 314:268-274(2006)
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-158;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.